An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid - PubMed (original) (raw)

doi: 10.1038/ni945. Epub 2003 Jun 6.

Masahito Hashimoto, Yasuo Horie, Junya Masumoto, Su Qiu, Lisa Saab, Yasunori Ogura, Akiko Kawasaki, Koichi Fukase, Shoichi Kusumoto, Miguel A Valvano, Simon J Foster, Tak W Mak, Gabriel Nuñez, Naohiro Inohara

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An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid

Mathias Chamaillard et al. Nat Immunol. 2003 Jul.

Abstract

Nucleotide-binding oligomerization domain protein 1 (NOD1) belongs to a family that includes multiple members with NOD and leucine-rich repeats in vertebrates and plants. NOD1 has been suggested to have a role in innate immune responses, but the mechanism involved remains unknown. Here we report that NOD1 mediates the recognition of peptidoglycan derived primarily from Gram-negative bacteria. Biochemical and functional analyses using highly purified and synthetic compounds indicate that the core structure recognized by NOD1 is a dipeptide, gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP). Murine macrophages deficient in NOD1 did not secrete cytokines in response to synthetic iE-DAP and did not prime the lipopolysaccharide response. Thus, NOD1 mediates selective recognition of bacteria through detection of iE-DAP-containing peptidoglycan.

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